Amyloid fibrils are misfolded proteins that form ordered aggregates characterized by extensive â-sheet structure. Natural amyloids are most often found linked to diseases such as Alzheimer's and Parkinson's. Once formed, these fibril structures are usually temperature and pH stabilized over the native peptide conformation. In vitro studies have shown that amyloid-like fibrils can be formed from many different protein and polypeptide sequences with the appropriate solution conditions, indicating that fibril formation could be a general property of the peptide backbone. Due to their stability and sequence variety leading to different chemical functionality and fibril morphology, amyloid-like fibrils have potential nanotechnological applications. Our research here focuses on characterizing polyglutamic acid (PE) and a random polyglutamic acid/polyalanine (PEA) copolymer fibril formation, morphology, and surface chemistry through Thioflavin-T binding, AFM, and TEM. Additionally, we have studied the effect of seeding with both homo and heteropolymers on the morphology and kinetics of fibril formation. Finally, we have examined the ability of these fibrils to template CaCO3 formation and have analyzed the resulting composites through light microscopy and SEM.